Journal of Peptide Science 2005-03-01

Structure-activity studies on prolactin-releasing peptide (PrRP). Analogues of PrRP-(19-31)-peptide.

Robert G Boyle, Robert Downham, Tanmoy Ganguly, John Humphries, Jeff Smith, Stuart Travers

Index: J. Pept. Sci. 11 , 161-165, (2005)

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Abstract

An investigation of a series of single replacement analogues of PrRP-(19-31)-peptide has shown that good functional activity was retained when Phe31 was replaced with His(Bzl), Phe(4Cl), Nle, Trp, Cys(Bzl) or Glu(OBzl); when Val28 or Ile25 was replaced with Phg; when Gly24 was replaced with D-Ala, L-Ala, Pro or Sar; when Ser22 was replaced with Gly and when Ala21 was replaced with Thr or MeAla. The results confirm that the functionally important residues are located within the carboxyl terminal segment, -Ile-Arg-Pro-Val-Gly-Arg-Phe-NH2.Copyright (c) 2004 European Peptide Society and John Wiley & Sons, Ltd.